Triblock copolymers consisting of a silk-based ((Gly-Ala)3Gly-Glu) repeat flanked by hydrophilic outer blocks self-assemble
into micrometer long fibrils in response to a trigger. Since the exact mechanism of the fibril formation remains unclear,
we employ a multiscale modelling approach in combination with rare event simulations to elucidate key processes. Atomistic
scale simulations on the silk-based block suggest a mechanism in which a polypeptide prefolded into a β-roll structure docks
to the growing end of a fibril through the formation of Glu-Glu sidechain contacts. Subsequently it can slide to the optimal
position before water is expelled to form a dry interface between the fibril end and the attaching block copolymer. In addition,
we find that the folded state of the silk-based block is further stabilised through interactions with its neighboring block.
Templated folding may also play a role in case a partially folded polypeptide attaches. The coarse-grained simulations indicate
that the attachment and subsequent sliding is mediated by the hydrophilic flanks in a size dependent manner. The hydrophilic
blocks prevent random aggregation and allow growth only at the end of the fibril. Our multiscale approach may be used for
other fibril-forming peptides.

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